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Article ; Online: Measuring Antibacterial Autophagy.

Boyle, Keith B / Randow, Felix

Methods in molecular biology (Clifton, N.J.)

2019 Volume 1880, Page(s) 679–690

Abstract: Bacteria that escape from membrane-enclosed vacuoles to the cytosol of cells are targeted by autophagy, which recognizes and captures bacteria into autophagosomes wherein their proliferation is restricted. Here we discuss two means by which antibacterial ...

Abstract	Bacteria that escape from membrane-enclosed vacuoles to the cytosol of cells are targeted by autophagy, which recognizes and captures bacteria into autophagosomes wherein their proliferation is restricted. Here we discuss two means by which antibacterial autophagy is assessed: (1) the visualization and enumeration of autophagy protein recruitment to the vicinity of cytosolic bacteria by means of immunofluorescence microscopy and (2) the measurement of autophagy-dependent restriction of bacterial proliferation by means of colony-forming unit assay.
MeSH term(s)	Autophagosomes/immunology ; Autophagosomes/microbiology ; Autophagy/immunology ; Biological Assay/instrumentation ; Biological Assay/methods ; Cell Culture Techniques/instrumentation ; Cell Culture Techniques/methods ; Colony Count, Microbial/instrumentation ; Colony Count, Microbial/methods ; HeLa Cells ; Host-Pathogen Interactions/immunology ; Humans ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Microscopy, Fluorescence/instrumentation ; Microscopy, Fluorescence/methods ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; RNA Interference ; Salmonella typhimurium/genetics ; Salmonella typhimurium/immunology ; Salmonella typhimurium/isolation & purification ; Transformation, Bacterial ; Vacuoles/immunology ; Vacuoles/microbiology
Chemical Substances	Luminescent Proteins ; MAP1LC3A protein, human ; Microtubule-Associated Proteins
Language	English
Publishing date	2019-01-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8873-0_45
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Article ; Online: How cells deploy ubiquitin and autophagy to defend their cytosol from bacterial invasion.

Randow, Felix

Autophagy

2011 Volume 7, Issue 3, Page(s) 304–309

Abstract: Autophagy serves as a cell-autonomous effector mechanism of innate immunity in the cytosol. Autophagy restricts bacterial proliferation by separating bacteria from the nutrient-rich cytosol and delivering them into bactericidal autolysosomes. Autophagy ... ...

Abstract	Autophagy serves as a cell-autonomous effector mechanism of innate immunity in the cytosol. Autophagy restricts bacterial proliferation by separating bacteria from the nutrient-rich cytosol and delivering them into bactericidal autolysosomes. Autophagy also restricts inflammation by enclosing the membrane remnants of vacuoles from which bacteria have escaped. In contrast to starvation-induced autophagy, which engulfs cytosol nonspecifically, antibacterial autophagy is receptor-mediated and selective. Several distinct pathways of antibacterial autophagy have been identified recently, which can be triggered by either bacterial PAMPs, host-mediated modifications of bacteria-containing vacuoles, or cytosolic bacteria that have become decorated with ubiquitin. Ubiquitin-coated bacteria are sensed by p62, a promiscuous autophagy receptor required for the uptake of a variety of ubiquitin-marked autophagy substrates, and by NDP52, an autophagy receptor that, by associating with the immunoregulatory kinase TBK1, may serve a dedicated function in cytosolic immunity.
MeSH term(s)	Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Autophagy ; Bacteria/metabolism ; Cytosol/immunology ; Cytosol/microbiology ; Humans ; Models, Biological ; Ubiquitin/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Ubiquitin
Language	English
Publishing date	2011-03-01
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.4161/auto.7.3.14539
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Article ; Online: Strange New World: Bacteria Catalyze Ubiquitylation via ADP Ribosylation.

Komander, David / Randow, Felix

Cell host & microbe

2017 Volume 21, Issue 2, Page(s) 127–129

Abstract: Three recent papers, including one by Kotewicz et al. (2016) in this issue of Cell Host & Microbe, show that Legionella deploys a novel form of ubiquitylation to generate its replicative vacuole. Without E1 and E2 enzymes, SidE effectors ubiquitylate ... ...

Abstract	Three recent papers, including one by Kotewicz et al. (2016) in this issue of Cell Host & Microbe, show that Legionella deploys a novel form of ubiquitylation to generate its replicative vacuole. Without E1 and E2 enzymes, SidE effectors ubiquitylate serine residues in substrates via an ADP-ribosylated ubiquitin intermediate.
MeSH term(s)	Adenosine Diphosphate Ribose ; Bacteria ; Humans ; Serine ; Ubiquitin ; Ubiquitination
Chemical Substances	Ubiquitin ; Adenosine Diphosphate Ribose (20762-30-5) ; Serine (452VLY9402)
Language	English
Publishing date	2017-02-09
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2017.01.014
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Article ; Online: Comparative study of GBP recruitment on two cytosol-dwelling pathogens, Francisella novicida and Shigella flexneri highlights differences in GBP repertoire and in GBP1 motif requirements.

Valeva, Stanimira V / Degabriel, Manon / Michal, Fanny / Gay, Gabrielle / Rohde, John R / Randow, Felix / Lagrange, Brice / Henry, Thomas

Pathogens and disease

2023 Volume 81

Abstract: Guanylate-Binding Proteins are interferon-inducible GTPases that play a key role in cell autonomous responses against intracellular pathogens. Despite sharing high sequence similarity, subtle differences among GBPs translate into functional divergences ... ...

Abstract	Guanylate-Binding Proteins are interferon-inducible GTPases that play a key role in cell autonomous responses against intracellular pathogens. Despite sharing high sequence similarity, subtle differences among GBPs translate into functional divergences that are still largely not understood. A key GBP feature is the formation of supramolecular GBP complexes on the bacterial surface. Such complexes are observed when GBP1 binds lipopolysaccharide (LPS) from Shigella and Salmonella and further recruits GBP2-4. Here, we compared GBP recruitment on two cytosol-dwelling pathogens, Francisella novicida and S. flexneri. Francisella novicida was coated by GBP1 and GBP2 and to a lower extent by GBP4 in human macrophages. Contrary to S. flexneri, F. novicida was not targeted by GBP3, a feature independent of T6SS effectors. Multiple GBP1 features were required to promote targeting to F. novicida while GBP1 targeting to S. flexneri was much more permissive to GBP1 mutagenesis suggesting that GBP1 has multiple domains that cooperate to recognize F. novicida atypical LPS. Altogether our results indicate that the repertoire of GBPs recruited onto specific bacteria is dictated by GBP-specific features and by specific bacterial factors that remain to be identified.
MeSH term(s)	Humans ; Cytosol/metabolism ; Cytosol/microbiology ; Shigella flexneri/genetics ; Shigella flexneri/metabolism ; Lipopolysaccharides ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism
Chemical Substances	Lipopolysaccharides ; GTP-Binding Proteins (EC 3.6.1.-) ; GBP1 protein, human
Language	English
Publishing date	2023-03-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2049-632X
ISSN (online)	2049-632X
DOI	10.1093/femspd/ftad005
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Article ; Online: CALCOCO2/NDP52 initiates selective autophagy through recruitment of ULK and TBK1 kinase complexes.

Boyle, Keith B / Ravenhill, Benjamin J / Randow, Felix

Autophagy

2019 Volume 15, Issue 9, Page(s) 1655–1656

Abstract: The selective macroautophagy of prospective cargo necessitates activity of the autophagy machinery at cargo-determined locations. Whether phagophore membranes are recruited to, or are ... ...

Abstract	The selective macroautophagy of prospective cargo necessitates activity of the autophagy machinery at cargo-determined locations. Whether phagophore membranes are recruited to, or are generated
MeSH term(s)	Autophagy ; Cytoplasm ; Macroautophagy ; Prospective Studies ; Protein Serine-Threonine Kinases
Chemical Substances	Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2019-07-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2019.1628548
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Article ; Online: Rubicon swaps autophagy for LAP.

Boyle, Keith B / Randow, Felix

Nature cell biology

2015 Volume 17, Issue 7, Page(s) 843–845

Abstract: Phagocytic cells engulf their prey into vesicular structures called phagosomes, of which a certain proportion becomes demarcated for enhanced maturation by a process called LC3-associated phagocytosis (LAP). Light has now been shed on the molecular ... ...

Abstract	Phagocytic cells engulf their prey into vesicular structures called phagosomes, of which a certain proportion becomes demarcated for enhanced maturation by a process called LC3-associated phagocytosis (LAP). Light has now been shed on the molecular requirements of LAP, establishing a central role for the protein Rubicon in the immune response to Aspergillus fumigatus.
MeSH term(s)	Animals ; Autophagy ; Female ; Intracellular Signaling Peptides and Proteins/metabolism ; Male ; Membrane Glycoproteins/metabolism ; Microtubule-Associated Proteins/metabolism ; NADPH Oxidases/metabolism ; Phagocytosis
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Membrane Glycoproteins ; Microtubule-Associated Proteins ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2015-06-30
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb3197
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 12: Show issues

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Article ; Online: Transbilayer Movement of Sphingomyelin Precedes Catastrophic Breakage of Enterobacteria-Containing Vacuoles.

Ellison, Cara J / Kukulski, Wanda / Boyle, Keith B / Munro, Sean / Randow, Felix

Current biology : CB

2020 Volume 30, Issue 15, Page(s) 2974–2983.e6

Abstract: Pathogenic bacteria enter the cytosol of host cells through uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the vacuolar membrane [1]. Bacterial invaders are sensed either directly, through cytosolic pattern-recognition ... ...

Abstract	Pathogenic bacteria enter the cytosol of host cells through uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the vacuolar membrane [1]. Bacterial invaders are sensed either directly, through cytosolic pattern-recognition receptors specific for bacterial ligands, or indirectly, through danger receptors that bind host molecules displayed in an abnormal context, for example, glycans on damaged BCVs [2-4]. In contrast to damage caused by Listeria monocytogenes, a Gram-positive bacterium, BCV rupture by Gram-negative pathogens such as Shigella flexneri or Salmonella Typhimurium remains incompletely understood [5, 6]. The latter may cause membrane damage directly, when inserting their Type Three Secretion needles into host membranes, or indirectly through translocated bacterial effector proteins [7-9]. Here, we report that sphingomyelin, an abundant lipid of the luminal leaflet of BCV membranes, and normally absent from the cytosol, becomes exposed to the cytosol as an early predictive marker of BCV rupture by Gram-negative bacteria. To monitor subcellular sphingomyelin distribution, we generated a live sphingomyelin reporter from Lysenin, a sphingomyelin-specific toxin from the earthworm Eisenia fetida [10, 11]. Using super resolution live imaging and correlative light and electron microscopy (CLEM), we discovered that BCV rupture proceeds through two distinct successive stages: first, sphingomyelin is gradually translocated into the cytosolic leaflet of the BCV, invariably followed by cytosolic exposure of glycans, which recruit galectin-8, indicating bacterial entry into the cytosol. Exposure of sphingomyelin on BCVs may therefore act as an early danger signal alerting the cell to imminent bacterial invasion.
MeSH term(s)	Cell Membrane/metabolism ; Cell Membrane/microbiology ; Cell Membrane/pathology ; Cytosol/metabolism ; Cytosol/microbiology ; Enterobacteriaceae/pathogenicity ; Galectins/metabolism ; Humans ; Polysaccharides/adverse effects ; Polysaccharides/metabolism ; Sphingomyelins/adverse effects ; Sphingomyelins/metabolism ; Vacuoles/metabolism ; Vacuoles/microbiology ; Vacuoles/pathology
Chemical Substances	Galectins ; LGALS8 protein, human ; Polysaccharides ; Sphingomyelins
Language	English
Publishing date	2020-07-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2020.05.083
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Zs.A 3208: Show issues

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Article ; Online: Self and nonself: how autophagy targets mitochondria and bacteria.

Randow, Felix / Youle, Richard J

Cell host & microbe

2014 Volume 15, Issue 4, Page(s) 403–411

Abstract: Autophagy is an evolutionarily conserved pathway that transports cytoplasmic components for degradation into lysosomes. Selective autophagy can capture physically large objects, including cell-invading pathogens and damaged or superfluous organelles. ... ...

Abstract	Autophagy is an evolutionarily conserved pathway that transports cytoplasmic components for degradation into lysosomes. Selective autophagy can capture physically large objects, including cell-invading pathogens and damaged or superfluous organelles. Selectivity is achieved by cargo receptors that detect substrate-associated "eat-me" signals. In this Review, we discuss basic principles of selective autophagy and compare the "eat-me" signals and cargo receptors that mediate autophagy of bacteria and bacteria-derived endosymbionts-i.e., mitochondria.
MeSH term(s)	Animals ; Autophagy/immunology ; Bacteria/immunology ; Humans ; Lysosomes/metabolism ; Mitochondria/metabolism ; Mitophagy ; Signal Transduction/immunology
Language	English
Publishing date	2014-04-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2014.03.012
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Article ; Online: TECPR1 conjugates LC3 to damaged endomembranes upon detection of sphingomyelin exposure.

Boyle, Keith B / Ellison, Cara J / Elliott, Paul R / Schuschnig, Martina / Grimes, Krista / Dionne, Marc S / Sasakawa, Chihiro / Munro, Sean / Martens, Sascha / Randow, Felix

The EMBO journal

2023 Volume 42, Issue 17, Page(s) e113012

Abstract: Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans ... ...

Abstract	Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin-8 triggers anti-bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta-propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N-terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent-exposed tryptophan (W154) essential for binding to sphingomyelin-positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12-E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin-specific TECPR1, in an arrangement reminiscent of certain multi-subunit ubiquitin E3 ligases.
MeSH term(s)	Animals ; Sphingomyelins ; Microtubule-Associated Proteins/metabolism ; Autophagy-Related Proteins/metabolism ; Carrier Proteins/metabolism ; Autophagy ; Ubiquitin-Protein Ligases/metabolism ; Autophagy-Related Protein 5/metabolism ; Mammals
Chemical Substances	Sphingomyelins ; Microtubule-Associated Proteins ; Autophagy-Related Proteins ; Carrier Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Autophagy-Related Protein 5
Language	English
Publishing date	2023-07-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2022113012
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 100: Show issues

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Article ; Online: Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection.

Otten, Elsje G / Werner, Emma / Crespillo-Casado, Ana / Boyle, Keith B / Dharamdasani, Vimisha / Pathe, Claudio / Santhanam, Balaji / Randow, Felix

Nature

2021 Volume 594, Issue 7861, Page(s) 111–116

Abstract: Ubiquitylation is a widespread post-translational protein modification in eukaryotes and marks bacteria that invade the cytosol as cargo for antibacterial ... ...

Abstract	Ubiquitylation is a widespread post-translational protein modification in eukaryotes and marks bacteria that invade the cytosol as cargo for antibacterial autophagy
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Animals ; Autophagy ; Cell Line ; HeLa Cells ; Humans ; Lipopolysaccharides/immunology ; Lipopolysaccharides/metabolism ; Mice ; RING Finger Domains ; Salmonella Infections/immunology ; Salmonella Infections/metabolism ; Salmonella Infections/microbiology ; Salmonella typhimurium ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Lipopolysaccharides ; Ubiquitin ; RNF213 protein, human (EC 2.3.2.27) ; RNF213 protein, mouse (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2021-05-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-021-03566-4
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
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